Bulldog Bio PNGase F PRIME Glycosidase


PNGase F PRIME Glycosidase

PNGase F PRIME is a mutant recombinant PNGase F cloned from Flavobacterium meningosepticum and expressed and purified from E. coli. The proprietary changes made to PNGase F advance processivity and access to cleavage sites. This turbo-charged enzyme has been shown to have unique characteristics when compared to other commercially-available sources of PNGase F. Data generated by independent outside researchers and companies shows that PRIME works on native glycoproteins and serum glycoproteins in minutes at room temperature. This advancement benefits applications that seek to understand glycobiology in a natural milieu. Glycan analysis of the digestion products shows that PNGase F PRIME digestion led to more complete glycan release and also allowed for the cleavage of glycans not released by the commercially-available enzymes when used at the same concentrations with the same digestion conditions. Preliminary data indicates that PNGase F PRIME has a higher specificity towards complex (tri and tetra-antennary) sialylated structures compared to the commercially sourced enzyme. Additionally, the work presented in this Analytical Chemistry paper utilized PNGase F PRIME for all in situ tissue work as the commercially-available PNGase enzymes did not work on native tissue to allow glycan recognition.





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